TPA primes alpha 2 beta 1 integrins for cell adhesion

: Tulla M, Helenius J, Jokinen J, Taubenberger A, Muller DJ, Heino J

Publisher: ELSEVIER SCIENCE BV

: 2008

: FEBS Letters

: FEBS LETTERS

: FEBS LETT

: 582

: 23-24

: 3520

: 3524

: 5

: 0014-5793

DOI: https://doi.org/10.1016/j.febslet.2008.09.022

Integrin avidity is regulated by changes in the conformation of the heterodimer and cluster formation. We measured cell adhesion by integrin alpha 2 beta 1 (CHO-alpha 2) to collagen at short contact times (0.5-60 s) by single cell force spectroscopy (SCFS). The adhesion increased rapidly with contact time and was further strengthened by the addition of 12-O-tetradecanoylphorbol-13- acetate (TPA), a protein kinase C (PKC) and integrin activator. TPA also improved the strength of adhesive units. Furthermore, changes in membrane nanotube properties indicated better coupling of integrins to the cell cytoskeleton. We conclude that in addition to increasing integrin avidity TPA strengthens integrin-cytoskeletal linkage.